ID I1I273_BRADI Unreviewed; 289 AA.
AC I1I273;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
GN Name=100821832 {ECO:0000313|EnsemblPlants:KQJ95721};
GN ORFNames=BRADI_3g18690v3 {ECO:0000313|EMBL:KQJ95721.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQJ95721};
RN [1] {ECO:0000313|EMBL:KQJ95721.1, ECO:0000313|EnsemblPlants:KQJ95721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ95721.1,
RC ECO:0000313|EnsemblPlants:KQJ95721};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ95721.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ95721.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ95721}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ95721};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or
CC endotransglycosylation (XET). Cleaves and religates xyloglucan
CC polymers, an essential constituent of the primary cell wall, and
CC thereby participates in cell wall construction of growing tissues.
CC {ECO:0000256|RuleBase:RU361120}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|RuleBase:RU361120}. Secreted, extracellular space,
CC apoplast {ECO:0000256|RuleBase:RU361120}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000256|RuleBase:RU361120}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC {ECO:0000256|RuleBase:RU361120}.
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DR EMBL; CM000882; KQJ95721.1; -; Genomic_DNA.
DR RefSeq; XP_003573588.1; XM_003573540.3.
DR AlphaFoldDB; I1I273; -.
DR STRING; 15368.I1I273; -.
DR GlyCosmos; I1I273; 1 site, No reported glycans.
DR EnsemblPlants; KQJ95721; KQJ95721; BRADI_3g18690v3.
DR GeneID; 100821832; -.
DR Gramene; KQJ95721; KQJ95721; BRADI_3g18690v3.
DR KEGG; bdi:100821832; -.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; I1I273; -.
DR OMA; FRSKKTC; -.
DR OrthoDB; 337487at2759; -.
DR Proteomes; UP000008810; Chromosome 3.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016762; F:xyloglucan:xyloglucosyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR CDD; cd02176; GH16_XET; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR044791; Beta-glucanase/XTH.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR008263; GH16_AS.
DR InterPro; IPR010713; XET_C.
DR InterPro; IPR016455; XTH.
DR PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR PANTHER; PTHR31062:SF40; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF06955; XET_C; 1.
DR PIRSF; PIRSF005604; XET; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|RuleBase:RU361120};
KW Cell wall {ECO:0000256|RuleBase:RU361120};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU361120};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361120};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361120};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Secreted {ECO:0000256|RuleBase:RU361120};
KW Signal {ECO:0000256|RuleBase:RU361120};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|RuleBase:RU361120"
FT CHAIN 28..289
FT /note="Xyloglucan endotransglucosylase/hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361120"
FT /id="PRO_5013982812"
FT DOMAIN 13..220
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005604-2"
SQ SEQUENCE 289 AA; 32828 MW; 89E11FAAF7B1F5A9 CRC64;
MGQARVHLLA SLVAFYLIVL AITQVTANLL DDFNNLWGNT KVVYDSTGQQ TIAMTLDRST
TSGFSSKSTY LFGRIDMDIK LVPGNSAGTV TTFYMVTEGP WQYHDEIDLE FLGNSSGNPY
TLHTNMFARG KGAREKRYNL WFDPTQDFHT YTIIWNQQFI RILIDDKLIR QIKNQLVYGV
PYPSYQPMRV FSSIWNADDW ATQGGRVKTD WSQAPFTAYF RNFKATSCSP SQSKICGQSS
LTGGGLFNQD LDETRKQQLK DVDANYKVYD YCTDSTRFQN GAPKECGLQ
//
